ID A0A1A6HND4_NEOLE Unreviewed; 349 AA.
AC A0A1A6HND4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE Flags: Fragment;
GN ORFNames=A6R68_22039 {ECO:0000313|EMBL:OBS79759.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS79759.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS79759.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS79759.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS79759.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00000251,
CC ECO:0000256|RuleBase:RU610713};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|RuleBase:RU610713}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS79759.1}.
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DR EMBL; LZPO01018093; OBS79759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6HND4; -.
DR STRING; 56216.A0A1A6HND4; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF17; HYALURONIDASE PH-20; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR PRINTS; PR00848; SPERMPH20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW Hydrolase {ECO:0000256|RuleBase:RU610713};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124}.
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT DISULFID 224..238
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT NON_TER 349
FT /evidence="ECO:0000313|EMBL:OBS79759.1"
SQ SEQUENCE 349 AA; 40338 MW; 210D20ACE70CEC41 CRC64;
MGGLRVKHLY WGSFVESGGT FQSVLIIFLL IPCSLTVDYR AIPLLPNETF LWIWNVPTEA
CIGQFNHSID LSLFPLIGSP RKTATGQPVT LFYVDRLGYY PHIDTRMREH HGGIPQLGNL
QNHLTKARTD IEHYIPVDRL GLAVIDWEEW RPTWLRNWRP KDIYRNKSID LVQANNAGIS
ISDATRQAKS AFEAAGRQFM EETLRLGKSV RPKYLWGYYL FPDCYNNKFQ DPNYDGKCPN
VEKQRNDDLS WMWRESTGLY PSVYLKRDLK SNRQATLYVR FRVVESIRVS KVRNESDPVP
IFVYTRLVFT DNITEYLLEE DLVNTIGEIV ALGPAGIIIW DAMTLAQRA
//